RESTRAINED LEAST SQUARES REFINEMENT OF NATIVE (CALCIUM) AND CADMIUM-SUBSTITUTED CARP PARVALBUMIN USING X-RAY CRYSTALLOGRAPHIC DATA AT 1.6-ANGSTROMS RESOLUTION
HOH 132 IS THE SEVENTH LIGAND FOR CA 109.
Restrained least squares refinement of native (calcium) and cadmium-substituted carp parvalbumin using X-ray crystallographic data at 1.6-A resolution.
The Coordination Polyhedron of Ca2+,Cd2+ in Parvalbumin
Refinement of the Structure of Carp Muscle Calcium-Binding Parvalbumin by Model Building and Difference Fourier Analysis
Terbium Replacement of Calcium in Carp Muscle Calcium-Binding Parvalbumin,an X-Ray Crystallographic Study
Troponin and Parvalbumin Calcium Binding Regions Predicted in Myosin Light Chain and T4 Lysozyme
Calcium Binding Proteins and Natural Membranes
The Coordination of Calcium Ions by Carp Muscle Calcium-Binding Proteins A,B,and C
Carp Muscle Calcium-Binding Protein, I.Characterization of the Tryptic Peptides and the Complete Amino Acid Sequence of Component B
Carp Muscle Calcium-Binding Protein, II.Structure Determination and General Description
Carp Muscle Calcium-Binding Protein, III.Phase Refinement Using the Tangent Formula
Gene Duplication in Carp Muscle Calcium Binding Protein
Gene Triplication Deduced from the Tertiary Structure of a Muscle Calcium Binding Protein
Structure of a Calcium Binding Carp Myogen
The Structure of a Calcium-Binding Protein from Carp Muscle
(ACE)AFAGVLNDADIAAALEACKAADSFNHKAFFAKVGLTSKSADDVKKAFAIIDQDKSGFIEEDELKLFLQNFKADAR ALTDGETKTFLKAGDSDGDGKIGVDEFTALVKA
XAFAGVLNDADIAAALEACKAADSFNHKAFFAKVGLTSKSADDVKKAFAIIDQDKSGFIEEDELKLFLQNFKADARALTD GETKTFLKAGDSDGDGKIGVDEFTALVKA
AFAGVLNDADIAAALEACKAADSFNHKAFFAKVGLTSKSADDVKKAFAIIDQDKSGFIEEDELKLFLQNFKADARALTDG ETKTFLKAGDSDGDGKIGVDEFTALVKA